ID   A0A3P8NHB8_ASTCA        Unreviewed;       701 AA.
AC   A0A3P8NHB8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=SMURF2 {ECO:0000313|Ensembl:ENSACLP00000004053.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000004053.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000004053.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000004053.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; A0A3P8NHB8; -.
DR   Ensembl; ENSACLT00000004140.1; ENSACLP00000004053.1; ENSACLG00000002616.1.
DR   GeneTree; ENSGT00940000155563; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265100; Chromosome 6.
DR   Bgee; ENSACLG00000002616; Expressed in liver and 8 other cell types or tissues.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd08382; C2_Smurf-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..94
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          203..236
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          249..282
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          367..701
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        669
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   701 AA;  80008 MW;  F6EF9A9EE71B2D46 CRC64;
     LAKKDFFRLP DPFAKVVVDG SGQCHSTDTV RNTLDPKWNQ HYDLYIGKSD SITISVWNHK
     KIHKKQGAGF LGCVRLLSNA INRLKDTGYQ RLDLNKLGPN DNDTVRGQIV VSLQSRDRIG
     SGGPVVDCSR LFDNDLPDGP ASEYSSPSGR PLSCVVDENT PVMTPVNGAE ASGPPGEQRI
     QERRVRSQRH RNYMSRTHLH TPPDLPEGYE QRTTQQGQVY FLHTQTGVST WHDPRVPRDL
     SNVNCEELGP LPPGWEIRNT ATGRVYFVDH NNRTTQFTDP RLSANLHPTQ LKEQVAPGGP
     QQALSPAQLP EEAECLTVPK YKRDLVQKLK ILRQELSQHQ PQAGHCRIEV SREEIFEESY
     RQVMKMRPKD LWKRLMIKFR GEEGLDYGGV AREWLYLLSH EMLNPYYGLF QYSRDDIYTL
     QINPDSAVNP EHLSYFHFVG RIMGMAVFHG HYIDGGFTLP FYKQLLGKPI TLDDMESVDP
     DLHNSLVWIL DNDITGVLDH TFCVEHNAYG EIIPHELKPN GKSISVTEDT KKEYVRLYVN
     WRFLHGIEAQ FLALQKGFNE VIPQHLLKSF DEKELELIVC GLGKIDIADW KSNTRLKHCT
     PDTNIVKWFW KAVESFDEER RARLLQFVTG SSRVPLQGFK ALQGAAGPRL FTIHQIDANT
     NNLPKAHTCF NRIDIPPYES YDKLYDKLLT AIEETCGFAV E
//